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Metal-Binding protein - DOAJ

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Last Updated: 16 January 2022

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The Small Metal-Binding Protein SmbP Simplifies the Recombinant Expression and Purification of the Antimicrobial Peptide LL-37

We'll discuss LL-37 tagged with SmbP, a relatively new carrier protein that enhances the production of recombinant proteins and peptides in Escherichia coli due to its importance. Methods: A DNA construct of SmbP_LL-37 was converted into E. coli BL21 after overnight expression, the protein was purified directly from the cell lysate using immobilized metal-affinity chromatography. Using the colony forming unit assay technique, the antimicrobial activity of both SmbP-37 and free LL-37 was determined. SmbP-37 was discovered in the cell lysate's soluble fraction, and after purification with IMAC, protein gel electrophoresis, and analysis by ImageJ, it revealed 90% purity. SmbP_LL-37, a total of 3. 6 grams, was created from one liter of cell culture. Both SmbP_LL-37 and free LL-37 demonstrated inhibition against Staphylococcus aureus and Escherichia coli. Conclusions: The SmbP fusion protein is a useful tool for the manufacture of biologically active LL-37 peptide.

Source link: https://doi.org/10.3390/antibiotics10101271

* Please keep in mind that all text is summarized by machine, we do not bear any responsibility, and you should always check original source before taking any actions

* Please keep in mind that all text is summarized by machine, we do not bear any responsibility, and you should always check original source before taking any actions